1DXO

Crystal structure of human NAD[P]H-QUINONE oxidoreductase CO with 2,3,5,6,tetramethyl-P-benzoquinone (duroquinone) at 2.5 Angstrom resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Spacegroup name	P 1
Unit cell lengths	55.579, 56.912, 97.755
Unit cell angles	76.24, 76.73, 86.33

Refinement procedure

Resolution	27.660 - 2.500
R-factor	0.202
Rwork	0.202
R-free	0.26400
Structure solution method	OTHER
RMSD bond length	0.010
RMSD bond angle	21.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS (0.9)
Refinement software	CNS (0.9)

Data quality characteristics

	Overall
Low resolution limit [Å]	27.660
High resolution limit [Å]	2.500
Rmerge	0.044 *
Number of reflections	36969
Completeness [%]	93.8
Redundancy	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8 *	25 *	pH 8.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-15 (mg/ml)
2	1	drop	Tris-HCl	25 (mM)
3	1	drop	FAD	0.005 (mM)
4	1	reservoir	PEG3350	30 (%)
5	1	reservoir	sodium acetate	200 (mM)
6	1	reservoir	sodium tricine	100 (mg/ml)
7	1	reservoir	FAD	0.012-0.024 (mM)
8	1	reservoir	duroquinone	8.9 (mM)
9	1	reservoir	NADH	0.025 (mM)